[English] 日本語
Yorodumi- PDB-1qlt: STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qlt | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE | ||||||
Components | VANILLYL-ALCOHOL OXIDASE | ||||||
Keywords | FLAVOENZYME / OXIDOREDUCTASE / FLAVOPROTEIN / METHANOL UTILIZATION / PEROXISOME / OXIDASE / CATALYSIS | ||||||
Function / homology | Function and homology information vanillyl-alcohol oxidase / vanillyl-alcohol oxidase activity / methanol metabolic process / FAD binding / peroxisome Similarity search - Function | ||||||
Biological species | PENICILLIUM SIMPLICISSIMUM (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.2 Å | ||||||
Authors | Mattevi, A. / Fraaije, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1999 Title: Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase. Authors: Fraaije, M.W. / van den Heuvel, R.H. / van Berkel, W.J. / Mattevi, A. #1: Journal: Proteins: Struct.,Funct., Genet. / Year: 1997 Title: Crystallization and Preliminary X-Ray Analysis of the Flavoenzyme Vanillyl-Alcohol Oxidase from Penicillium Simplicissimum Authors: Mattevi, A. / Fraaije, M.W. / Coda, A. / Van Berkel, W.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1qlt.cif.gz | 229.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1qlt.ent.gz | 191.5 KB | Display | PDB format |
PDBx/mmJSON format | 1qlt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ql/1qlt ftp://data.pdbj.org/pub/pdb/validation_reports/ql/1qlt | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.232426, -0.972447, 0.018018), Vector: Details | BIOLOGICAL_UNIT: OCTAMER | |
-Components
#1: Protein | Mass: 62939.910 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) PENICILLIUM SIMPLICISSIMUM (fungus) / Description: FUNGUS / Cellular location: INTRACELLULARGlossary of biology / Organelle: PEROXISOMESPeroxisome / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P56216, aryl-alcohol oxidase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Method: vapor diffusion, hanging drop / pH: 4.6 / Details: FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging dropDetails: Mattevi, A., (1997) Proteins: Struct.,Funct., Genet., 27, 601. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1998 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 55414 / % possible obs: 93.1 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Rmerge(I) obs: 0.089 / Rsym value: 0.089 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.2→2.3 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.226 / Mean I/σ(I) obs: 2.8 / Rsym value: 0.226 / % possible all: 78.8 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 285553 |
Reflection shell | *PLUS % possible obs: 78.8 % |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: OTHER / Resolution: 2.2→30 Å / Cross valid method: THROUGHOUT / σ(F): 0
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→30 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.21 / Rfactor Rwork: 0.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|